ADAM11

ADAM11

ADAM metallopeptidase domain 11, also known as ADAM11, is a human gene.cite web | title = Entrez Gene: ADAM11 ADAM metallopeptidase domain 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4185| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. This gene represents a candidate tumor supressor gene for human breast cancer based on its location within a minimal region of chromosome 17q21 previously defined by tumor deletion mapping.cite web | title = Entrez Gene: ADAM11 ADAM metallopeptidase domain 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4185| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Wolfsberg TG, Primakoff P, Myles DG, White JM |title=ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. |journal=J. Cell Biol. |volume=131 |issue= 2 |pages= 275–8 |year= 1995 |pmid= 7593158 |doi=
*cite journal | author=Katagiri T, Harada Y, Emi M, Nakamura Y |title=Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 39–44 |year= 1994 |pmid= 7956356 |doi=
*cite journal | author=Emi M, Katagiri T, Harada Y, "et al." |title=A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. |journal=Nat. Genet. |volume=5 |issue= 2 |pages= 151–7 |year= 1994 |pmid= 8252040 |doi= 10.1038/ng1093-151
*cite journal | author=Sagane K, Ohya Y, Hasegawa Y, Tanaka I |title=Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 and MDC3: novel human cellular disintegrins highly expressed in the brain. |journal=Biochem. J. |volume=334 ( Pt 1) |issue= |pages= 93–8 |year= 1998 |pmid= 9693107 |doi=
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8
*cite journal | author=Brandenberger R, Wei H, Zhang S, "et al." |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971
*cite journal | author=Fu GK, Wang JT, Yang J, "et al." |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205–10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем решить контрольную работу

Look at other dictionaries:

  • Matrix metalloproteinase — Cell surface associated MT1 MMP (MMP14), Green fluorescent protein (GFP) fused to the C term produces a signal on the surface of the cell[1] Matrix metalloproteinases (MMPs) are zinc dependent endopeptidases; other family members are adamalysins …   Wikipedia

  • Metalloendopeptidase — A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. External links MeSH Metalloendopeptidase 3.4.21 24: Endopeptidase …   Wikipedia

  • Collagenase — matrix metallopeptidase 1 (interstitial collagenase) Identifiers Symbol MMP1 Entrez 4312 HUGO …   Wikipedia

  • ADAM17 — ADAM metallopeptidase domain 17 PDB rendering based on 1bkc …   Wikipedia

  • Neprilysin — Membrane metallo endopeptidase The structure of the neprilysin ectodomain in complex with a zinc chelating inhibitor. The zinc atom is shown as a gray sphere and the inhibitor is shown in green. Rendering based on 1r1h …   Wikipedia

  • Pregnancy-associated plasma protein A — Pregnancy associated plasma protein A, pappalysin 1 Identifiers Symbols PAPPA; ASBABP2; DIPLA1; IGFBP 4ase; PAPA; PAPP A; PAPPA1 External IDs …   Wikipedia

  • MMP14 — Matrix metallopeptidase 14 (membrane inserted) PDB rendering based on 1bqq …   Wikipedia

  • MMP1 — Matrix metallopeptidase 1 (interstitial collagenase) PDB rendering based on 1ayk …   Wikipedia

  • MMP3 — Matrix metallopeptidase 3 (stromelysin 1, progelatinase) PDB rendering based on 1b3d …   Wikipedia

  • MMP7 — Matrix metallopeptidase 7 (matrilysin, uterine) PDB rendering based on 1mmp …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”